한빛사논문
Yujin Lee1,2,5, Junho Choe3,4,5, Ok Hyun Park1,2, Yoon Ki Kim1,2,*
1 Creative Research Initiatives Center for Molecular Biology of Translation, Korea University, Seoul 02841, Republic of Korea
2 Division of Life Sciences, Korea University, Seoul 02841, Republic of Korea
3 Department of Life Science, College of Natural Sciences, Hanyang University, Seoul 04763, Republic of Korea
4 Research Institute for Natural Sciences, Hanyang University, Seoul 04763, Republic of Korea
5 These authors contributed equally to this work.
*Correspondence : Yoon Ki Kim
Abstract
N6-Methyladenosine (m6A), the most prevalent internal modification associated with eukaryotic mRNAs, influences many steps of mRNA metabolism, including splicing, export, and translation, as well as stability. Recent studies have revealed that m6A-containing mRNAs undergo one of two distinct pathways of rapid degradation: deadenylation via the YT521-B homology (YTH) domain-containing family protein 2 (YTHDF2; an m6A reader protein)–CCR4/NOT (deadenylase) complex or endoribonucleolytic cleavage by the YTHDF2–HRSP12–ribonuclease (RNase) P/mitochondrial RNA-processing (MRP) (endoribonuclease) complex. Some m6A-containing circular RNAs (circRNAs) are also subject to endoribonucleolytic cleavage by YTHDF2–HRSP12–RNase P/MRP. Here, we highlight recent progress on the molecular mechanisms underlying rapid mRNA degradation via m6A and describe our current understanding of the dynamic regulation of m6A-mediated mRNA decay through the crosstalk between m6A (or YTHDF2) and other cellular factors.
Keywords : m6A modification; YTHDF2; HRSP12; RNase P/MRP; circular RNA; endoribonucleolytic cleavage
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